On the propagation of the OH radical produced by Cu-amyloid beta peptide model complexes. Insight from molecular modelling

Metallomics ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 1765-1780
Author(s):  
Federica Arrigoni ◽  
Fabio Rizza ◽  
Renata Tisi ◽  
Luca De Gioia ◽  
Giuseppe Zampella ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Molecular Modelling ◽  
Amyloid Beta Peptide ◽  
Side Chains ◽  
Oh Radical ◽  
Ros Production ◽  
Aβ Peptide ◽  
Model Complexes ◽  
Beta Peptide ◽  
Amyloid Aβ

Alzheimer's disease involves an anomalous interaction of copper with the amyloid Aβ peptide, inducing ROS production. The propagation of the OH radical toward Aβ side chains is investigated by molecular modelling.

scholarly journals Accumulation of Innate Amyloid Beta Peptide in Glioblastoma Tumors

2019 ◽  
Vol 20 (10) ◽  
pp. 2482 ◽  
Author(s):  
Lilia Y. Kucheryavykh ◽  
Jescelica Ortiz-Rivera ◽  
Yuriy V. Kucheryavykh ◽  
Astrid Zayas-Santiago ◽  
Amanda Diaz-Garcia ◽  
...  
Keyword(s):  
Blood Vessels ◽  
Amyloid Beta ◽  
Glioma Cells ◽  
Amyloid Beta Peptide ◽  
Enzyme Linked Immunosorbent Assay ◽  
Aβ Peptide ◽  
Brain Areas ◽  
Aβ Peptides ◽  
Beta Peptide ◽  
Glioma Tumors

Immunostaining with specific antibodies has shown that innate amyloid beta (Aβ) is accumulated naturally in glioma tumors and nearby blood vessels in a mouse model of glioma. In immunofluorescence images, Aβ peptide coincides with glioma cells, and enzyme-linked immunosorbent assay (ELISA) have shown that Aβ peptide is enriched in the membrane protein fraction of tumor cells. ELISAs have also confirmed that the Aβ(1–40) peptide is enriched in glioma tumor areas relative to healthy brain areas. Thioflavin staining revealed that at least some amyloid is present in glioma tumors in aggregated forms. We may suggest that the presence of aggregated amyloid in glioma tumors together with the presence of Aβ immunofluorescence coinciding with glioma cells and the nearby vasculature imply that the source of Aβ peptides in glioma can be systemic Aβ from blood vessels, but this question remains unresolved and needs additional studies.

Self-assembly characteristics of a structural analogue of Tjernberg peptide

RSC Advances ◽  
2014 ◽  
Vol 4 (32) ◽  
pp. 16517-16523 ◽  
Author(s):  
Keerthana Ramaswamy ◽  
Priyadharshini Kumaraswamy ◽  
Swaminathan Sethuraman ◽  
Uma Maheswari Krishnan
Keyword(s):  
Amyloid Beta ◽  
Self Assembly ◽  
Amyloid Plaques ◽  
Amyloid Beta Peptide ◽  
Side Chains ◽  
Structural Analogue ◽  
Beta Peptide

This article aims to understand the pathogenesis behind the formation of amyloid plaques using a modified version of the KLVFF peptide. It was found that the cytotoxicity of the nanostructures formed by the RIVFF peptide may be attributed to the aminoacids with long side chains along with hydrophobic aminoacids resembling the amyloid beta peptide.

G-lymphatic, vascular and immune pathways for Aβ clearance cascade and therapeutic targets for Alzheimer’s disease

2020 ◽  
Vol 23 ◽  
Author(s):  
Saurav Chakraborty ◽  
Jyothsna ThimmaReddygari ◽  
Divakar Selvaraj
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Amyloid Beta ◽  
Complement System ◽  
Therapeutic Targets ◽  
Neuronal Cell ◽  
Precursor Protein ◽  
Amyloid Beta Peptide ◽  
Beta Peptide ◽  
Immune Pathways

The Alzheimer disease is a age related neurodegenerative disease. The factors causing alzheimer disease are numerous. Research on humans and rodent models predicted various causative factors involved in Alzheimer disease progression. Among them, neuroinflammation, oxidative stress and apoptosis play a major role because of accumulation of extracellular amyloid beta peptides. Here, the clearance of amyloid beta peptide plays a major role because of the imbalance in the production and clearance of the amyloid beta peptide. Additionally, neuroinflammation by microglia, astrocytes, cytokines, chemokines and the complement system also have a major role in Alzheimer disease. The physiological clearance pathways involved in amyloid beta peptide are glymphatic, vascular and immune pathways. Amyloid precursor protein, low density lipoprotein receptor-related protein 1, receptor for advanced glycation end product, apolipoprotein E, clusterin, aquaporin 4, auto-antibodies, complement system, cytokines and microglia are involved in amyloid beta peptide clearance pathways across the blood brain barrier. The plaque formation in the brain by alternative splicing of amyloid precursor protein and production of misfolded protein results in amyloid beta agglomeration. This insoluble amyloid beta leads to neurodegenerative cascade and neuronal cell death occurs. Studies had shown disturbed sleep may be a risk factor for dementia and cognitive decline. In this review, the therapeutic targets for alzheimer disease via focussing on pathways for amyloid beta clearance are discussed.

Conformations and Biological Activities of Amyloid Beta Peptide 25-35

2009 ◽  
Vol 999 (999) ◽  
pp. 1-6 ◽  
Author(s):  
L. Millucci ◽  
L. Ghezzi ◽  
G. Bernardini ◽  
A. Santucci
Keyword(s):  
Amyloid Beta ◽  
Biological Activities ◽  
Amyloid Beta Peptide ◽  
Beta Peptide
Sign in / Sign up

Export Citation Format

Share Document